Participation of adenosine diphosphate in regulation of the 2-oxoglutarate dehydrogenase complex from human heart.
Adenosine diphosphate (ADP) increases the activity of the highly purified 2-oxoglutarate dehydrogenase complex (OGDC) from human heart. The degree of activation is higher at low 2-oxoglutarate concentrations. The OGDC-catalyzed reaction rate versus ADP concentration curve is S-shaped at unsaturating substrate concentration. This is a catalytic attribute of cooperativity of the sites for binding of the allosteric effector ADP.
Ostrovtsova
S A
SA
Laboratory of Enzymology and Biotechnology, Institute of Biochemistry, Academy of Sciences of the Byelorussian SSR, Grodno.
Strumilo
S A
SA
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D001665:Binding Sites; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D066298:In Vitro Techniques; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*
D000244:Adenosine Diphosphate; D007655:Ketoglutarate Dehydrogenase Complex